RELATION BETWEEN ATPASE ACTIVITY AND LIGHT-CHAINS OF MYOSIN IN DEVELOPING, ADULT AND DENERVATED MUSCLES OF SEVERAL ANIMAL SPECIES

  • 1 January 1976
    • journal article
    • research article
    • Vol. 25  (4) , 295-+
Abstract
Fast, slow and cardiac muscles of the rat, guinea-pig, cat, rabbit and chick were studied by a sodium dodecyl sulfate polyacrylamide gel electrophoresis. In normal adult muscles the electrophoretic pattern of L chains of myosin reflected the myosin ATPase activity only when muscles from the same animal species were compared. In homologous muscles from adult animals differing in size, the size-dependent difference in myosin ATPase activity was not revealed in the electrophoretic pattern. In developing and denervated muscle, changes in myosin ATPase activity were connected with changes in the pattern of light chains of myosin or this pattern did not change. This relation was different in fast and slow muscles and differed in chick and rabbit muscles. There were several explanations of the relation between ATPase activity of myosin and the pattern of L chains of myosin. Myosin from the soleus muscle of 1 mo. old rabbit contained L chains corresponding to fast and slow type of myosin. The change in myosin ATPase activity during development was due to changes in the ratio between the fast and slow type of myosin.

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